P0DN29 · AMYG_ARTBC

Function

Catalytic activity

  • Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose.
    EC:3.2.1.3 (UniProtKB | ENZYME | Rhea)

Features

Showing features for binding site, active site.

161050100150200250300350400450500550600
Type
IDPosition(s)Description
Binding site143substrate
Active site199Proton acceptor
Active site202Proton donor

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentextracellular region
Cellular Componentfungal-type vacuole
Molecular Functionglucan 1,4-alpha-glucosidase activity
Molecular Functionstarch binding
Biological Processpolysaccharide catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Glucoamylase ARB_02327-1
  • EC number
  • Alternative names
    • 1,4-alpha-D-glucan glucohydrolase
    • Allergen sch c 1 homolog
    • Glucan 1,4-alpha-glucosidase

Gene names

    • ORF names
      ARB_02327-1

Organism names

Accessions

  • Primary accession
    P0DN29
  • Secondary accessions
    • D4B1J8

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Allergenic properties

May cause an allergic reaction in human.

Keywords

PTM/Processing

Features

Showing features for signal, propeptide, chain, glycosylation, disulfide bond.

Type
IDPosition(s)Description
Signal1-18
PropeptidePRO_000043442119-24
ChainPRO_000043442225-610Glucoamylase ARB_02327-1
Glycosylation49N-linked (GlcNAc...) asparagine
Glycosylation194N-linked (GlcNAc...) asparagine
Disulfide bond233↔236
Disulfide bond245↔472
Disulfide bond285↔293

Keywords

Expression

Induction

Expression is up-regulated in presence of human keratinocytes.

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain504-610CBM20

Sequence similarities

Belongs to the glycosyl hydrolase 15 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    610
  • Mass (Da)
    67,485
  • Last updated
    2015-10-14 v1
  • Checksum
    2B0CBC8F4769E795
MRVTSLLWSSLVIPAAVGFQVRFKPSEDTALDTVDDGTLQSLLDNIGLNGSNAWDTRPGLVIASPSKKDPNYFFTWTRDSALVLKCITDAFAAGNTALQETIHEYISSQARIQLLNTRSGGLSSGGLGEPKYRVDETPYNEDWGRPQADGPALRATALIAYARWLLENDYYDVAKSIVWPVVKNDLSYVSEHWNTTAFDLWEEVNSPSFFTTIVQHRALVEGINIARALDETCPHCESQAPQALCYLQSYWTGTAVRSNYGQGRSGLDVASILGSIHTFDPEGECDDTTFQPCSARALANHKAVTDSFRSIYKINGGIKQGEAVAVGRYPEDVYFNGNPWYLATYAAAEQLYDAMYQWNKIGKITVTDVSMPFFKDIYPEVQTGTHESSSPEFGNIIAAVKAYAEGYIEVAKKYTPCTGMLSEQFSRDNGTPLSVADLTWSYASYLTVMARRNSVVPASWGEKNARDIPSTCVPSSATGPYQTATITHWPPNLTPTAQPSPCPTALPTKNNVRFRLLATTQVGEDVFLVGSIPELGSWDVKKAVPLNADIYADNCHQWYVDIELPTAVAFEYKFIRKRGGEVVWEQDPNRKYTVPQTCGVSGAIKRDTWR

Sequence caution

The sequence EFE30837.1 differs from that shown. Reason: Erroneous gene model prediction The predicted gene has been split into 2 genes: ARB_02327-1 and ARB_02327-2.

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
ABSU01000026
EMBL· GenBank· DDBJ
EFE30837.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.

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